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CAZyme Information: THC90997.1

You are here: Home > Sequence: THC90997.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aspergillus tanneri
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
CAZyme ID THC90997.1
CAZy Family GH1
CAZyme Description Alpha-glucosidase [Source:UniProtKB/TrEMBL;Acc:A0A4S3J9S8]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
804 89467.25 5.6481
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AtanneriNIH1004 13590 N/A 33 13557
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.20:20

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 274 486 1.9e-47 0.4098360655737705

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395838 Glyco_hydro_31 2.35e-113 272 681 2 442
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
269888 GH31_MGAM_SI_GAA 1.03e-107 290 595 1 356
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase. This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).
224418 YicI 7.11e-74 57 721 22 709
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269889 GH31_GANC_GANAB_alpha 1.95e-60 290 721 1 467
neutral alpha-glucosidase C, neutral alpha-glucosidase AB. This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.
269890 GH31_glucosidase_II_MalA 2.11e-49 290 598 1 334
Alpha-glucosidase II-like. Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 27 760 31 932
0.0 20 773 20 954
8.45e-287 27 792 33 990
3.51e-286 27 792 35 991
4.81e-286 27 792 33 990

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.44e-93 64 722 44 801
Sugar beet alpha-glucosidase with acarbose [Beta vulgaris],3W38_A Sugar beet alpha-glucosidase [Beta vulgaris],3WEL_A Sugar beet alpha-glucosidase with acarviosyl-maltotriose [Beta vulgaris],3WEM_A Sugar beet alpha-glucosidase with acarviosyl-maltotetraose [Beta vulgaris],3WEN_A Sugar beet alpha-glucosidase with acarviosyl-maltopentaose [Beta vulgaris],3WEO_A Sugar beet alpha-glucosidase with acarviosyl-maltohexaose [Beta vulgaris]
2.62e-78 63 722 54 785
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-acetyl-cysteine [Homo sapiens]
2.62e-78 63 722 54 785
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA [Homo sapiens],5NN5_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin [Homo sapiens],5NN6_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-hydroxyethyl-1-deoxynojirimycin [Homo sapiens],5NN8_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with acarbose [Homo sapiens]
2.70e-78 63 722 56 787
Crystal structure of human GAA [Homo sapiens],5KZX_A Crystal structure of human GAA [Homo sapiens]
2.40e-77 65 754 53 811
Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase [Homo sapiens],2QMJ_A Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose [Homo sapiens],3CTT_A Crystal complex of N-terminal Human Maltase-Glucoamylase with Casuarine [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.42e-263 27 759 28 932
Alpha-glucosidase OS=Aspergillus niger OX=5061 GN=aglA PE=1 SV=1
8.05e-263 20 759 24 932
Alpha-glucosidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=agdA PE=2 SV=1
6.90e-176 6 759 5 898
Glucoamylase 1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=GAM1 PE=1 SV=3
3.59e-172 33 759 42 910
Glucoamylase 1 OS=Schwanniomyces occidentalis OX=27300 GN=GAM1 PE=1 SV=1
4.98e-168 62 759 60 918
Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=agl1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000528 0.999446 CS pos: 23-24. Pr: 0.5768

TMHMM  Annotations      help

There is no transmembrane helices in THC90997.1.